This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jimenez, N.
Right arrow Articles by Tomás, J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jimenez, N.
Right arrow Articles by Tomás, J. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 2009, p. 2228-2236, Vol. 191, No. 7
0021-9193/09/$08.00+0     doi:10.1128/JB.01395-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Genetics and Proteomics of Aeromonas salmonicida Lipopolysaccharide Core Biosynthesis{triangledown} ,{dagger}

Natalia Jimenez,1 Anna Lacasta,1 Silvia Vilches,1 Mercé Reyes,1 Judit Vazquez,1 Eleonora Aquillini,2 Susana Merino,1 Miguel Regué,2 and Juan M. Tomás1*

Departamento de Microbiología, Facultad de Biología, Universidad de Barcelona, Diagonal 645, 08071 Barcelona,1 Departamento de Microbiología y Parasitología Sanitarias, Facultad de Farmacia, Universidad de Barcelona, Av. Joan XXIII s/n, 08028 Barcelona, Spain2

Received 6 October 2008/ Accepted 2 January 2009

Comparison between the lipopolysaccharide (LPS) core structures of Aeromonas salmonicida subsp. salmonicida A450 and Aeromonas hydrophila AH-3 shows great similarity in the inner LPS core and part of the outer LPS core but some differences in the distal part of the outer LPS core (residues LD-Hep, D-Gal, and D-GalNAc). The three genomic regions encoding LPS core biosynthetic genes in A. salmonicida A450, of which regions 2 and 3 have genes identical to those of A. hydrophila AH-3, were fully sequenced. A. salmonicida A450 region 1 showed seven genes: three identical to those of A. hydrophila AH-3, three similar but not identical to those of A. hydrophila AH-3, and one without any homology to any well-characterized gene. A. salmonicida A450 mutants with alterations in the genes that were not identical to those of A. hydrophila AH-3 were constructed, and their LPS core structures were fully elucidated. At the same time, all the A. salmonicida A450 genes identical to those of A. hydrophila AH-3 were used to complement the previously obtained A. hydrophila AH-3 mutants for each of these genes. Combining the gene sequence and complementation test data with the structural data and phenotypic characterization of the mutant LPSs enabled a presumptive assignment of all LPS core biosynthesis gene functions in A. salmonicida A450. Furthermore, hybridization studies with internal probes for the A. salmonicida-specific genes using different A. salmonicida strains (strains of different subspecies or atypical strains) showed a unique or prevalent LPS core type, which is the one fully characterized for A. salmonicida A450.


* Corresponding author. Mailing address: Departamento Microbiología, Facultad Biología, Universidad Barcelona, Diagonal 645, 08071 Barcelona, Spain. Phone: 34-93-4021486. Fax: 34-93-4039047. E-mail: jtomas{at}ub.edu

{triangledown} Published ahead of print on 16 January 2009.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.


Journal of Bacteriology, April 2009, p. 2228-2236, Vol. 191, No. 7
0021-9193/09/$08.00+0     doi:10.1128/JB.01395-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Jimenez, N., Vilches, S., Lacasta, A., Regue, M., Merino, S., Tomas, J. M. (2009). A Bifunctional Enzyme in a Single Gene Catalyzes the Incorporation of GlcN into the Aeromonas Core Lipopolysaccharide. J. Biol. Chem. 284: 32995-33005 [Abstract] [Full Text]